BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 30284

Title: Backbone structure of the Yersinia pestis outer membrane protein Ail in phospholipid bilayer nanodisc

Authors: Dutta, S.; Yong, Y.; Marassi, F.

Citation: Dutta, S.; Yong, Y.; Marassi, F.. "Backbone structure of the Yersinia pestis outer membrane protein Ail in phospholipid bilayer nanodisc"  . ., .-..

Assembly members:
entity_1, polymer, 156 residues, 17492.400 Da.

Natural source:   Common Name: Yersinia pestis   Taxonomy ID: 632   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Yersinia pestis

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
entity_1: EGESSISIGYAQSRVKEDGY KLDKNPRGFNLKYRYEFNND WGVIGSFAQTRRGFEESVDG FKLIDGDFKYYSVTAGPVFR INEYVSLYGLLGAGHGKAKF SSIFGQSESRSKTSLAYGAG LQFNPHPNFVIDASYEYSKL DDVKVGTWMLGAGYRF

Data sets:
Data typeCount
13C chemical shifts94
15N chemical shifts91
1H chemical shifts91

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 156 residues - 17492.400 Da.

1   GLUGLYGLUSERSERILESERILEGLYTYR
2   ALAGLNSERARGVALLYSGLUASPGLYTYR
3   LYSLEUASPLYSASNPROARGGLYPHEASN
4   LEULYSTYRARGTYRGLUPHEASNASNASP
5   TRPGLYVALILEGLYSERPHEALAGLNTHR
6   ARGARGGLYPHEGLUGLUSERVALASPGLY
7   PHELYSLEUILEASPGLYASPPHELYSTYR
8   TYRSERVALTHRALAGLYPROVALPHEARG
9   ILEASNGLUTYRVALSERLEUTYRGLYLEU
10   LEUGLYALAGLYHISGLYLYSALALYSPHE
11   SERSERILEPHEGLYGLNSERGLUSERARG
12   SERLYSTHRSERLEUALATYRGLYALAGLY
13   LEUGLNPHEASNPROHISPROASNPHEVAL
14   ILEASPALASERTYRGLUTYRSERLYSLEU
15   ASPASPVALLYSVALGLYTHRTRPMETLEU
16   GLYALAGLYTYRARGPHE

Samples:

sample_1: Ail, [U-13C; U-15N; U-2H], 0.66 mM; DMPC 49.5 mM; DMPG 16.5 mM; sodium chloride 5 mM; sodium phosphate 25 mM

sample_conditions_1: ionic strength: 10 mM; pH: 6.5; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D TROSY-HNCAsample_1isotropicsample_conditions_1
3D 15N-NOESYsample_1isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

TOPSPIN, Bruker Biospin - processing

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

NMR spectrometers:

  • Bruker AvanceIII 800 MHz
  • Bruker Avance 600 MHz

Related Database Links: